Evidence map›Paper›PMID 39122699›Full record

ArticleNature communications2024

A synthetic peptide mimic kills Candida albicans and synergistically prevents infection.

Sebastian Schaefer, Raghav Vij, Jakob L Sprague, Sophie Austermeier, Hue Dinh, Peter R Judzewitsch, Sven Müller-Loennies, Taynara Lopes Silva, Eric Seemann, Britta Qualmann and 9 more

Abstract read
In one paragraph

Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

14 citing papers in PubMed.

  1. Article
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  4. Review
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  6. Article
  7. EnhancedDrug delivery · 2025
    Article
  8. Article
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  12. Article
  13. Article
  14. Characterization of glycogen-related glycoside hydrolaseFrontiers in cellular and infection microbiology · 2024
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

19 authors.

Sebastian SchaeferSchool of Chemical Engineering, University of New South Wales (UNSW), Sydney, NSW, Australia.ORCID 0000-0003-3166-1998
Raghav VijDepartment of Microbial Pathogenicity Mechanisms, Leibniz Institute for Natural Product Research and Infection Biology, Hans Knoell Institute, Jena, Germany.ORCID 0000-0001-5812-0484
Jakob L SpragueDepartment of Microbial Pathogenicity Mechanisms, Leibniz Institute for Natural Product Research and Infection Biology, Hans Knoell Institute, Jena, Germany.ORCID 0000-0003-0756-803X
Sophie AustermeierDepartment of Microbial Pathogenicity Mechanisms, Leibniz Institute for Natural Product Research and Infection Biology, Hans Knoell Institute, Jena, Germany.ORCID 0000-0002-1048-5983
Hue DinhARC Centre of Excellence in Synthetic Biology, School of Natural Sciences, Macquarie University, North Ryde, NSW, Australia.ORCID 0000-0003-3455-3394
Peter R JudzewitschSchool of Chemical Engineering, University of New South Wales (UNSW), Sydney, NSW, Australia.
Sven Müller-LoenniesDivision of Biophysics, Research Center Borstel, Leibniz Lung Center, Borstel, Germany.ORCID 0000-0002-3375-9721
Taynara Lopes SilvaDepartment of Biomolecular Chemistry, Leibniz Institute for Natural Product Research and Infection Biology, Hans Knoell Institute, Jena, Germany.
Eric SeemannInstitute of Biochemistry I, Jena University Hospital - Friedrich Schiller University Jena, Jena, Germany.ORCID 0000-0002-3270-1253
Britta QualmannInstitute of Biochemistry I, Jena University Hospital - Friedrich Schiller University Jena, Jena, Germany.ORCID 0000-0002-5743-5764
Christian HertweckDepartment of Biomolecular Chemistry, Leibniz Institute for Natural Product Research and Infection Biology, Hans Knoell Institute, Jena, Germany.ORCID 0000-0002-0367-337X
Kirstin ScherlachDepartment of Biomolecular Chemistry, Leibniz Institute for Natural Product Research and Infection Biology, Hans Knoell Institute, Jena, Germany.ORCID 0000-0002-1326-3761
Thomas GutsmannDivision of Biophysics, Research Center Borstel, Leibniz Lung Center, Borstel, Germany.
Amy K CainARC Centre of Excellence in Synthetic Biology, School of Natural Sciences, Macquarie University, North Ryde, NSW, Australia.ORCID 0000-0002-4230-6572
Nathaniel CorriganSchool of Chemical Engineering, University of New South Wales (UNSW), Sydney, NSW, Australia.
Mark S GresnigtCluster of Excellence Balance of the Microverse, Friedrich Schiller University Jena, Jena, Germany.ORCID 0000-0002-9514-4634
Cyrille BoyerSchool of Chemical Engineering, University of New South Wales (UNSW), Sydney, NSW, Australia. cboyer@unsw.edu.au.ORCID 0000-0002-4564-4702
Megan D LenardonSchool of Biotechnology and Biomolecular Sciences, UNSW, Sydney, NSW, Australia. m.lenardon@unsw.edu.au.ORCID 0000-0002-9471-7402
Sascha BrunkeDepartment of Microbial Pathogenicity Mechanisms, Leibniz Institute for Natural Product Research and Infection Biology, Hans Knoell Institute, Jena, Germany. sascha.brunke@leibniz-hki.de.ORCID 0000-0001-7740-4570

Funding

Bundesministerium für Bildung und Forschung (Federal Ministry of Education and Research) 16GW0238KDeutsche Forschungsgemeinschaft (German Research Foundation) 210879364Deutsche Forschungsgemeinschaft (German Research Foundation) 434385622 / GR 5617/1-1Deutsche Forschungsgemeinschaft (German Research Foundation) 446404928Deutsche Forschungsgemeinschaft (German Research Foundation) QU116/9-1EC | Horizon 2020 Framework Programme (EU Framework Programme for Research and Innovation H2020) 847507
6 · The paper itself

Abstract

More than two million people worldwide are affected by life-threatening, invasive fungal infections annually. Candida species are the most common cause of nosocomial, invasive fungal infections and are associated with mortality rates above 40%. Despite the increasing incidence of drug-resistance, the development of novel antifungal formulations has been limited. Here we investigate the antifungal mode of action and therapeutic potential of positively charged, synthetic peptide mimics to combat Candida albicans infections. Our data indicates that these synthetic polymers cause endoplasmic reticulum stress and affect protein glycosylation, a mode of action distinct from currently approved antifungal drugs. The most promising polymer composition damaged the mannan layer of the cell wall, with additional membrane-disrupting activity. The synergistic combination of the polymer with caspofungin prevented infection of human epithelial cells in vitro, improved fungal clearance by human macrophages, and significantly increased host survival in a Galleria mellonella model of systemic candidiasis. Additionally, prolonged exposure of C. albicans to the synergistic combination of polymer and caspofungin did not lead to the evolution of tolerant strains in vitro. Together, this work highlights the enormous potential of these synthetic peptide mimics to be used as novel antifungal formulations as well as adjunctive antifungal therapy.

Indexed as

Antifungal AgentsCandida albicansCandidiasisCaspofunginDrug SynergismPeptidesAnimalsCell WallEndoplasmic Reticulum StressEpithelial CellsHumansMacrophagesMannansMicrobial Sensitivity TestsMothsPolymersAntifungal AgentsCaspofunginMannansPeptidesPolymers

Identifiers

PMID39122699
PMCPMC11315985

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.